Reynolds_2015_Biochem.J_468_17

Reference

Title : Pseudoproteases: mechanisms and function - Reynolds_2015_Biochem.J_468_17
Author(s) : Reynolds SL , Fischer K
Ref : Biochemical Journal , 468 :17 , 2015
Abstract :

Catalytically inactive enzymes (also known as pseudoproteases, protease homologues or paralogues, non-peptidase homologues, non-enzymes and pseudoenzymes) have traditionally been hypothesized to act as regulators of their active homologues. However, those that have been characterized demonstrate that inactive enzymes have an extensive and expanding role in biological processes, including regulation, inhibition and immune modulation. With the emergence of each new genome, more inactive enzymes are being identified, and their abundance and potential as therapeutic targets has been realized. In the light of the growing interest in this emerging field the present review focuses on the classification, structure, function and mechanism of inactive enzymes. Examples of how inactivity is defined, how this is reflected in the structure, functions of inactive enzymes in biological processes and their mode of action are discussed.

PubMedSearch : Reynolds_2015_Biochem.J_468_17
PubMedID: 25940733

Related information

Citations formats

Reynolds SL, Fischer K (2015)
Pseudoproteases: mechanisms and function
Biochemical Journal 468 :17

Reynolds SL, Fischer K (2015)
Biochemical Journal 468 :17